Extended Data Fig. 7: The MD simulations of acyl donor substrates in the active sites of CsmA and BbmA. | Nature Chemistry

Extended Data Fig. 7: The MD simulations of acyl donor substrates in the active sites of CsmA and BbmA.

From: Structural insights into two thiamine diphosphate-dependent enzymes and their synthetic applications in carbon–carbon linkage reactions

Extended Data Fig. 7

(a)–(d), The binding models of CsmA with acyl donors IPA (S2, a), HPPA (S3, b), OPBA (S8, c), or 4-MOVA (S14, d) from the MD simulations. (e)–(h), The binding models of BbmA with acyl donors OPTA (S12, e), 4-MOVA (S14, f), CBOA (S17, g), or IPA (S2, h) from the MD simulations. The ThDP are shown as yellow sticks. Hydrogen bond interactions are shown as yellow dashed lines, and hydrophobic interactions within 4 Å are shown as black dashed lines.

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